Home

ACTC1 (human)

Overview ACTC1 Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others. Belongs to the actin family. Note: This description may include information from UniProtKB. Protein type: Myosin binding protein; Motility/polarity/chemotaxis; Cytoskeletal protein; Contractile protein; Cell development/differentiation Cellular Component: I band; sarcomere; cytoplasm; actin filament; cytosol Molecular Function: myosin binding; ATPase activity; ATP binding Biological Process: ATP catabolic process; response to drug; apoptosis; actin filament-based movement; muscle thin filament assembly; actomyosin structure organization and biogenesis; cardiac myofibril assembly; muscle filament sliding; response to ethanol; heart contraction; cardiac muscle morphogensis; actin-myosin filament sliding; cardiac muscle contraction Reference #:  P68032 (UniProtKB) Alt. Names/Synonyms: ACTC; ACTC1; Actin, alpha cardiac muscle 1; actin, alpha, cardiac muscle 1; Alpha-cardiac actin; ASD5; CMD1R; CMH11 Gene Symbols: ACTC1 Molecular weight: 42,019 Da Basal Isoelectric point: 5.23  Predict pI for various phosphorylation states CST Pathways:  Death Receptor Signaling Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below ACTC1

STRING  |  Scansite  |  Phospho.ELM  |  Pfam  |  ENZYME  |  DISEASE 102540 192600 612098 612794  |  Source  |  InnateDB  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	88		S35-p	APRAVFPsIVGRPRH
0	40		K52-a	VMVGMGQkDsyVGDE
0	105		K52-u	VMVGMGQkDsyVGDE
0	406		S54-p	VGMGQkDsyVGDEAQ
0	953		Y55-p	GMGQkDsyVGDEAQs
0	9		S62-p	yVGDEAQskRGILtL
0	169		K63-a	VGDEAQskRGILtLk
0	110		K63-u	VGDEAQskRGILtLk
0	8		T68-p	QskRGILtLkyPIEH
0	5		K70-a	kRGILtLkyPIEHGI
0	4		K70-m1	kRGILtLkyPIEHGI
0	45		K70-u	kRGILtLkyPIEHGI
0	20		Y71-p	RGILtLkyPIEHGII
0	2		T79-p	PIEHGIItNWDDMEk
0	1		K86-a	tNWDDMEkIWHHtFy
0	8		K86-u	tNWDDMEkIWHHtFy
0	10		T91-p	MEkIWHHtFyNELRV
0	736		Y93-p	kIWHHtFyNELRVAP
0	1		K115-a	TEAPLNPkANREKMT
0	14		K115-u	TEAPLNPkANREKMT
0	16		Y145-p	IQAVLSLyASGRTTG
0	91		Y168-p	VTHNVPIyEGyALPH
0	68		Y171-p	NVPIyEGyALPHAIM
0	2		T188-p	DLAGRDLtDyLMkIL
0	224		Y190-p	AGRDLtDyLMkILtE
0	6		K193-a	DLtDyLMkILtERGy
0	87		K193-u	DLtDyLMkILtERGy
0	20		T196-p	DyLMkILtERGysFV
0	194		Y200-p	kILtERGysFVTTAE
0	5		S201-p	ILtERGysFVTTAER
0	4		K215-a	REIVRDIkEkLCyVA
0	1		K217-m1	IVRDIkEkLCyVALD
0	1		K217	IVRDIkEKLCyVALD
0	16		Y220-p	DIkEkLCyVALDFEN
0	3		S235-p	EMATAASsSSLEksy
0	3		K240-u	ASsSSLEksyELPDG
0	9		S241-p	SsSSLEksyELPDGQ
0	20		Y242-p	sSSLEksyELPDGQV
0	14		T251-p	LPDGQVItIGNERFR
0	2		S267-p	PETLFQPsFIGMESA
0	12		Y281-p	AGIHETTyNSIMKCD
0	69		Y296-p	IDIRKDLyANNVLSG
0	61		Y308-p	LSGGTTMyPGIADRM
0	99		K317-u	GIADRMQkEItALAP
0	4		T320-p	DRMQkEItALAPsTM
0	6		S325-p	EItALAPsTMkIkII
0	4		K328-a	ALAPsTMkIkIIAPP
0	127		K328-u	ALAPsTMkIkIIAPP
0	6		K330-a	APsTMkIkIIAPPER
0	103		K330-u	APsTMkIkIIAPPER
0	17		Y364-p	MWISKQEyDEAGPSI

	mouse
S35-p	APRAVFPsIVGRPRH
K52-a	VMVGMGQkDsyVGDE
K52-u	VMVGMGQkDsyVGDE
S54-p	VGMGQkDsyVGDEAQ
Y55-p	GMGQkDsyVGDEAQs
S62-p	yVGDEAQskRGILtL
K63-a	VGDEAQskRGILtLk
K63-u	VGDEAQskRGILtLk
T68-p	QskRGILtLkyPIEH
K70	kRGILtLKyPIEHGI
K70	kRGILtLKyPIEHGI
K70-u	kRGILtLkyPIEHGI
Y71-p	RGILtLkyPIEHGII
T79-p	PIEHGIItNWDDMEk
K86	tNWDDMEKIWHHtFy
K86-u	tNWDDMEkIWHHtFy
T91-p	MEkIWHHtFyNELRV
Y93-p	kIWHHtFyNELRVAP
K115	TEAPLNPKANREKMT
K115-u	TEAPLNPkANREKMT
Y145-p	IQAVLSLyASGRTTG
Y168-p	VTHNVPIyEGyALPH
Y171-p	NVPIyEGyALPHAIM
T188-p	DLAGRDLtDyLMkIL
Y190-p	AGRDLtDyLMkILtE
K193-a	DLtDyLMkILtERGy
K193-u	DLtDyLMkILtERGy
T196-p	DyLMkILtERGysFV
Y200-p	kILtERGysFVTTAE
S201-p	ILtERGysFVTTAER
K215-a	REIVRDIkEkLCyVA
K217	IVRDIkEKLCyVALD
K217-u	IVRDIkEkLCyVALD
Y220-p	DIkEkLCyVALDFEN
S235-p	EMATAASsSSLEKsY
K240	ASsSSLEKsYELPDG
S241-p	SsSSLEKsYELPDGQ
Y242	sSSLEKsYELPDGQV
T251-p	LPDGQVItIGNERFR
S267-p	PETLFQPsFIGMESA
Y281-p	AGIHETTyNSIMKCD
Y296	IDIRKDLYANNVLSG
Y308	LSGGTTMYPGIADRM
K317-u	GIADRMQkEItALAP
T320-p	DRMQkEItALAPsTM
S325-p	EItALAPsTMkIkII
K328-a	ALAPsTMkIkIIAPP
K328-u	ALAPsTMkIkIIAPP
K330-a	APsTMkIkIIAPPER
K330-u	APsTMkIkIIAPPER
Y364-p	MWISKQEyDEAGPSI

	rat
S35	APRAVFPSIVGRPRH
K52	VMVGMGQKDsyVGDE
K52	VMVGMGQKDsyVGDE
S54-p	VGMGQKDsyVGDEAQ
Y55-p	GMGQKDsyVGDEAQS
S62	yVGDEAQSKRGILTL
K63	VGDEAQSKRGILTLK
K63	VGDEAQSKRGILTLK
T68	QSKRGILTLKYPIEH
K70	KRGILTLKYPIEHGI
K70	KRGILTLKYPIEHGI
K70	KRGILTLKYPIEHGI
Y71	RGILTLKYPIEHGII
T79	PIEHGIITNWDDMEK
K86	TNWDDMEKIWHHTFy
K86	TNWDDMEKIWHHTFy
T91	MEKIWHHTFyNELRV
Y93-p	KIWHHTFyNELRVAP
K115	TEAPLNPKANREKMT
K115	TEAPLNPKANREKMT
Y145	IQAVLSLYASGRTTG
Y168-p	VTHNVPIyEGyALPH
Y171-p	NVPIyEGyALPHAIM
T188	DLAGRDLTDyLMKIL
Y190-p	AGRDLTDyLMKILTE
K193	DLTDyLMKILTERGy
K193	DLTDyLMKILTERGy
T196	DyLMKILTERGySFV
Y200-p	KILTERGySFVTTAE
S201	ILTERGySFVTTAER
K215	REIVRDIKEKLCyVA
K217	IVRDIKEKLCyVALD
K217	IVRDIKEKLCyVALD
Y220-p	DIKEKLCyVALDFEN
S235	EMATAASSSSLEKsy
K240	ASSSSLEKsyELPDG
S241-p	SSSSLEKsyELPDGQ
Y242-p	SSSLEKsyELPDGQV
T251	LPDGQVITIGNERFR
S267	PETLFQPSFIGMESA
Y281	AGIHETTYNSIMKCD
Y296-p	IDIRKDLyANNVLSG
Y308-p	LSGGTTMyPGIADRM
K317	GIADRMQKEITALAP
T320	DRMQKEITALAPSTM
S325	EITALAPSTMKIKII
K328	ALAPSTMKIKIIAPP
K328	ALAPSTMKIKIIAPP
K330	APSTMKIKIIAPPER
K330	APSTMKIKIIAPPER
Y364	MWISKQEYDEAGPSI

Home  |  Curator Login With enhanced literature mining using Linguamatics I2E Produced by 3rd Millennium  |  Design by Digizyme ©2003-2013 Cell Signaling Technology, Inc.